| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| CC_0110 | dnaJ | CC_0110 | CC_0011 | Thioredoxin; Identified by match to protein family HMM. | dnaJ protein; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and Gr [...] | 0.644 |
| CC_0110 | dnaK | CC_0110 | CC_0010 | Thioredoxin; Identified by match to protein family HMM. | dnaK protein; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.543 |
| CC_0110 | ftsH | CC_0110 | CC_3226 | Thioredoxin; Identified by match to protein family HMM. | Cell division protein FtsH; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins; Belongs to the AAA ATPase family. In the central section; belongs to the AAA ATPase family. | 0.403 |
| CC_0110 | groL | CC_0110 | CC_0685 | Thioredoxin; Identified by match to protein family HMM. | Chaperonin, 60 kDa; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.895 |
| CC_0110 | groS | CC_0110 | CC_0686 | Thioredoxin; Identified by match to protein family HMM. | Chaperonin, 10 kDa; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.627 |
| CC_0110 | grpE | CC_0110 | CC_0154 | Thioredoxin; Identified by match to protein family HMM. | grpE protein; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent i [...] | 0.883 |
| CC_0110 | hslU | CC_0110 | CC_3728 | Thioredoxin; Identified by match to protein family HMM. | Heat shock protein HslU; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. | 0.877 |
| CC_0110 | hslV | CC_0110 | CC_3727 | Thioredoxin; Identified by match to protein family HMM. | Heat shock protein HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.883 |
| CC_0110 | lon | CC_0110 | CC_1960 | Thioredoxin; Identified by match to protein family HMM. | ATP-dependent protease LA; ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner (By similarity). CcrM is an important target of the Lon protease pathway in C.crescentus (By similarity). | 0.554 |
| CC_1031 | dnaJ | CC_1031 | CC_0011 | Hypothetical protein; Identified by Glimmer2; putative. | dnaJ protein; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and Gr [...] | 0.822 |
| CC_1031 | dnaK | CC_1031 | CC_0010 | Hypothetical protein; Identified by Glimmer2; putative. | dnaK protein; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.973 |
| CC_1031 | ftsH | CC_1031 | CC_3226 | Hypothetical protein; Identified by Glimmer2; putative. | Cell division protein FtsH; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins; Belongs to the AAA ATPase family. In the central section; belongs to the AAA ATPase family. | 0.457 |
| CC_1031 | groL | CC_1031 | CC_0685 | Hypothetical protein; Identified by Glimmer2; putative. | Chaperonin, 60 kDa; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.978 |
| CC_1031 | groS | CC_1031 | CC_0686 | Hypothetical protein; Identified by Glimmer2; putative. | Chaperonin, 10 kDa; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.904 |
| CC_1031 | grpE | CC_1031 | CC_0154 | Hypothetical protein; Identified by Glimmer2; putative. | grpE protein; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent i [...] | 0.865 |
| CC_1031 | hslU | CC_1031 | CC_3728 | Hypothetical protein; Identified by Glimmer2; putative. | Heat shock protein HslU; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. | 0.905 |
| CC_1031 | hslV | CC_1031 | CC_3727 | Hypothetical protein; Identified by Glimmer2; putative. | Heat shock protein HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.911 |
| CC_1031 | lon | CC_1031 | CC_1960 | Hypothetical protein; Identified by Glimmer2; putative. | ATP-dependent protease LA; ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner (By similarity). CcrM is an important target of the Lon protease pathway in C.crescentus (By similarity). | 0.856 |
| dnaJ | CC_0110 | CC_0011 | CC_0110 | dnaJ protein; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and Gr [...] | Thioredoxin; Identified by match to protein family HMM. | 0.644 |
| dnaJ | CC_1031 | CC_0011 | CC_1031 | dnaJ protein; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and Gr [...] | Hypothetical protein; Identified by Glimmer2; putative. | 0.822 |
